Purification and several properties of dihydroxyacetone kinase from the methylotrophic yeast Candida boidinii
Bystrykh, L.V.; Trotsenko, I.A.
Biokhimiia 48(10): 1611-1616
1983
ISSN/ISBN: 0320-9725 PMID: 6315084 Document Number: 217506
A procedure for isolation of a homogeneous dihydroxyacetone kinase including fractionation by polyethylene glycol and ion-exchange chromatography on polyethylenimine-Biogel has been developed. The enzyme is a dimer with Mr = 139 000 (2.71 000 according to SDS disc electrophoresis) and has a pI of 4.64 and pH optimum of 7.8-8.2. The enzyme phosphorylates dihydroxyacetone and, in a lesser degree, glyceraldehyde. ATP is the most efficient phosphate group donor for the enzyme. When ITP, GTP, CTP and UTP are used, the dihydroxyacetone kinase activity is about 30%.